| Year |
Citation |
Score |
| 1972 |
Rosenberry TL, Bernhard SA. Studies of catalysis by acetylcholinesterase. Synergistic effects of inhibitors during the hydrolysis of acetic acid esters Biochemistry. 11: 4308-4321. PMID 5079901 |
0.312 |
|
| 1965 |
Noller HF, Bernhard SA. Isolation and structural determination of chromophoric acyl peptides from subtilisin enzymes. Biochemistry. 4: 1118-1126. PMID 5839998 DOI: 10.1021/Bi00882A021 |
0.442 |
|
| 1965 |
Bernhard SA, Lau SJ, Noller H. Spectrophotometric identification of acyl enzyme intermediates. Biochemistry. 4: 1108-1118. PMID 5839997 DOI: 10.1021/Bi00882A020 |
0.483 |
|
| 1964 |
BERNHARD S, GRDINIC Z, NOLLER H, SHALTIEL N. PROPERTIES OF A BLOCKED TETRAPEPTIDE ANALOGUE OF THE ACTIVE SITE OF Proceedings of the National Academy of Sciences of the United States Of. 52: 1489-1494. PMID 14243523 DOI: 10.1073/Pnas.52.6.1489 |
0.404 |
|
| 1959 |
Bernhard SA, Orgel LE. Mechanism of enzyme inhibition by phosphate esters Science. 130: 625-626. PMID 13799750 DOI: 10.1126/Science.130.3376.625 |
0.479 |
|
| 1955 |
Bernhard SA. A simple model of molecular specificity in enzyme-substrate systems. II. The correlation of the michaelis constant with the inhibition constant Journal of the American Chemical Society. 77: 1973-1974. DOI: 10.1021/Ja01612A079 |
0.347 |
|
| 1955 |
Bernhard SA. A simple model of molecular specificity in enzyme-substrate systems. I. Theory and applications to the system acetylcholinesterase-substrate Journal of the American Chemical Society. 77: 1966-1972. DOI: 10.1021/Ja01612A078 |
0.313 |
|
| 1954 |
Bernhard SA, Garfield E, Hammett LP. Specific effects in acid catalysis by ion exchange resins. III. Some observations on the effect of polyvalent cations Journal of the American Chemical Society. 76: 991-992. DOI: 10.1021/Ja01633A013 |
0.603 |
|
| 1953 |
Bernhard SA, Hammett LP. Specific Effects in Acid Catalysis by Ion Exchange Resins. II. Hydrolysis of Esters in Water Solution1 Journal of the American Chemical Society. 75: 5834-5835. DOI: 10.1021/Ja01119A017 |
0.604 |
|
| 1953 |
Bernhard SA, Hammett LP. Specific effects in acid catalysis by ion exchange resins. I. Hydrolysis of esters in 70% aqueous acetone Journal of the American Chemical Society. 75: 1798-1800. DOI: 10.1021/Ja01104A006 |
0.61 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 1970 |
Bernhard SA, Gutfreund H. Steps in the reactions of proteolytic enzymes with their substrates. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 257: 105-110. PMID 4399037 DOI: 10.1098/Rstb.1970.0012 |
0.283 |
|
| 1973 |
Malhotra OP, Bernhard SA. Activation of a covalent enzyme substrate bond by noncovalent interaction with an effector Proceedings of the National Academy of Sciences of the United States of America. 70: 2074-2081. PMID 4352970 |
0.282 |
|
| 1981 |
Malhotra OP, Bernhard SA, Seydoux F. Structural and functional consequences of subunit interactions in glyceraldehyde 3-phosphate dehydrogenase Biochimie. 63: 131-141. PMID 7225460 DOI: 10.1016/S0300-9084(81)80177-0 |
0.272 |
|
| 1960 |
Bernhard SA, Coles WC, Nowell JF. Kinetics of the system α-chymotrypsin methyl hippurate water hydroxylamine: The role of water in enzymatic hydrolysis Journal of the American Chemical Society. 82: 3043-3050. DOI: 10.1021/Ja01497A018 |
0.271 |
|
| 1948 |
DAVIDSON D, BERNHARD SA. The structure of Meldrum's supposed beta-lactonic acid. Journal of the American Chemical Society. 70: 3426-8. PMID 18891879 DOI: 10.1021/Ja01190A060 |
0.271 |
|
| 1981 |
Odom TA, Chipman DM, Betts G, Bernhard SA. Transient and steady-state kinetic studies of sodium-potassium adenosine triphosphatase using β-(2-furyl)acryloyl phosphate as chromophoric substrate assay Biochemistry. 20: 480-486. PMID 6260131 DOI: 10.1021/Bi00506A006 |
0.267 |
|
| 1981 |
Malhotra OP, Bernhard SA. Role of nicotinamide adenine dinucleotide as an effector in formation and reactions of acylglyceraldehyde-3-phosphate dehydrogenase Biochemistry. 20: 5529-5538. PMID 7295691 |
0.262 |
|
| 1986 |
Weber JA, Turpin P, Bernhard SA, Peticolas WL. Chromophoric cinnamic acid substrates as resonance Raman probes of the active site environment in native and unfolded alpha-chymotrypsin. Biochemistry. 25: 1912-7. PMID 3707918 DOI: 10.1021/Bi00356A012 |
0.254 |
|
| 1968 |
Malhotra OP, Bernhard SA. Spectrophotometric identification of an active site-specific acyl glyceraldehyde 3-phosphate dehydrogenase. The regulation of its kinetic and equilibrium properties by coenzyme. Journal of Biological Chemistry. 243: 1243-1252. PMID 4296412 |
0.252 |
|
| 1952 |
Bernhard SA. The preparation of specific adsorbants Journal of the American Chemical Society. 74: 4946-4947. DOI: 10.1021/Ja01139A503 |
0.251 |
|
| 1988 |
Bernhard SA. The intracellular equilibrium thermodynamic and steady-state concentrations of metabolites Cell Biophysics. 12: 119-132. PMID 2453275 DOI: 10.1007/BF02918354 |
0.249 |
|
| 1982 |
Huskins KR, Bernhard SA, Dahlquist FW. Halibut muscle 3-phosphoglycerate kinase. Chemical and physical properties of the enzyme and its substrate complexes Biochemistry. 21: 4180-4188. PMID 6982068 DOI: 10.1021/Bi00260A041 |
0.241 |
|
| 1989 |
Malhotra OP, Bernhard SA. Noncovalent modulation by ATP of the acyl transfer from acyl-glyceraldehyde-3-phosphate dehydrogenase to phosphate Biochemistry. 28: 124-128. PMID 2706238 |
0.236 |
|
| 1974 |
Bernhard SA, Malhotra OP. Color, Conformation, and Catalysis Israel Journal of Chemistry. 12: 471-481. DOI: 10.1002/ijch.197400037 |
0.235 |
|
| 1985 |
Srivastava DK, Bernhard SA, Langridge R, McClarin JA. Molecular basis for the transfer of nicotinamide adenine dinucleotide among dehydrogenases Biochemistry. 24: 629-635. PMID 3158343 DOI: 10.1021/Bi00324A014 |
0.235 |
|
| 1980 |
Viratelle OM, Bernhard SA. Major component of acetylcholinesterase in Torpedo electroplax is not basal lamina associated Biochemistry. 19: 4999-5007. PMID 7459321 |
0.229 |
|
| 1982 |
Weber JP, Bernhard SA. Transfer of 1,3-diphosphoglycerate between glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase via an enzyme-substrate-enzyme complex. Biochemistry. 21: 4189-4194. PMID 7126536 |
0.228 |
|
| 1962 |
Bernhard SA, Berger A, Carter JH, Katchalski E, Sela M, Shalitin Y. Co-operative effects of functional groups in peptides. I. Aspartyl-serine derivatives Journal of the American Chemical Society. 84: 2421-2434. DOI: 10.1021/Ja00871A030 |
0.228 |
|
| 1986 |
Srivastava DK, Bernhard SA. Metabolite transfer via enzyme-enzyme complexes Science. 234: 1081-1086. PMID 3775377 |
0.225 |
|
| 1973 |
Matthews BW, Bernhard SA. Structure and symmetry of oligomeric enzymes. Annual Review of Biophysics and Bioengineering. 2: 257-317. PMID 4594848 |
0.22 |
|
| 1973 |
Matthews BW, Bernhard SA. Structure and symmetry of oligomeric enzymes. Annual Review of Biophysics and Bioengineering. 4: 257-317. PMID 4583656 DOI: 10.1146/annurev.bb.02.060173.001353 |
0.22 |
|
| 1984 |
Srivastava DK, Bernhard SA. Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde-3-phosphate dehydrogenase to liver alcohol dehydrogenase Biochemistry. 23: 4538-4545. PMID 6388629 |
0.218 |
|
| 1976 |
Schwendimann B, Ingbar D, Bernhard SA. On the function of half-site reactivity: Intersubunit NAD+-dependent activation of acyl-glyceraldehyde 3-phosphate dehydrogenase reduction by NADH Journal of Molecular Biology. 108: 123-138. PMID 187755 DOI: 10.1016/S0022-2836(76)80099-X |
0.215 |
|
| 1969 |
Dunn MF, Bernhard SA. Conjugate addition to activated β-arylacrylic acid derivatives. Thiolate anions Journal of the American Chemical Society. 91: 3274-3280. |
0.207 |
|
| 1960 |
Bernhard S, Gutfreund H. Mechanisms for Enzyme-Catalysed Transfer Reactions Progress in Biophysics and Biophysical Chemistry. 10: 115-152. DOI: 10.1016/s0096-4174(18)30188-4 |
0.204 |
|
| 1964 |
Bernhard SA, Shalitin Y, Tashjian ZH. The reaction of formohydroxamic acid with acyl derivatives in neutral aqueous solution Journal of the American Chemical Society. 86: 4406-4414. |
0.203 |
|
| 1986 |
Srivastava DK, Bernhard SA. Enzyme-enzyme interactions and the regulation of metabolic reaction pathways. Current Topics in Cellular Regulation. 28: 1-68. PMID 3539532 |
0.202 |
|
| 1985 |
Senear DF, Betts G, Bernhard SA. Multiple ion-dependent and substrate-dependent Na+/K+-ATPase conformational states. Transient and steady-state kinetic studies Biochemistry. 24: 6789-6798. PMID 3000437 DOI: 10.1021/Bi00345A010 |
0.199 |
|
| 1963 |
Bernhard SA, Bradley DF, Duda WL. Automatic Determination of Amino Acid Sequences Ibm Journal of Research and Development. 7: 246-251. DOI: 10.1147/rd.73.0246 |
0.192 |
|
| 1981 |
Kurzmack M, Inesi G, Tal N, Bernhard SA. Transient-state kinetic studies on the mechanism of furylacryloylphosphatase-coupled calcium ion transport with sarcoplasmic reticulum adenosine triphosphatase Biochemistry. 20: 486-491. PMID 6452157 DOI: 10.1021/Bi00506A007 |
0.191 |
|
| 1990 |
Bernhard SA, Tompa P. The mechanism of succinate or fumarate transfer in the tricarboxylic acid cycle allows molecular rotation of the intermediate Archives of Biochemistry and Biophysics. 276: 191-198. PMID 2297223 DOI: 10.1016/0003-9861(90)90026-U |
0.187 |
|
| 1966 |
Keizer J, Bernhard SA. The protonic equilibrium accompanying the acylation of chymotrypsin and subtilisin Biochemistry. 5: 4127-4136. |
0.17 |
|
| 1948 |
Davidson D, Bernhard SA. The structure of Meldrum's supposed β-lactonic acid Journal of the American Chemical Society. 70: 3426-3428. |
0.165 |
|
| 1971 |
Dunn MF, Bernhard SA. Rapid kinetic evidence for adduct formation between the substrate analog p-nitroso-N,N-dimethylaniline and reduced nicotinamide-adenine dinucleotide during enzymic reduction Biochemistry. 10: 4569-4575. PMID 4335090 |
0.164 |
|
| 1970 |
Rossi GL, Bernhard SA. Are the structure and function of an enzyme the same in aqueous solution and in the wet crystal? Journal of Molecular Biology. 49: 85-91. PMID 5450518 DOI: 10.1016/0022-2836(70)90377-3 |
0.164 |
|
| 1987 |
Srivastava DK, Bernhard SA. Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Transfer rates and equilibria with enzyme-enzyme complexes Biochemistry. 26: 1240-1246. PMID 3567170 |
0.158 |
|
| 1966 |
Shalitin Y, Bernhard SA. Cooperative effects of functional groups in peptides. II. Elimination reactions in aspartyl-(O-acyl)-serine derivatives Journal of the American Chemical Society. 88: 4711-4721. PMID 5918043 |
0.158 |
|
| 1989 |
Srivastava DK, Smolen P, Betts GF, Fukushima T, Spivey HO, Bernhard SA. Direct transfer of NADH between α-glycerol phosphate dehydrogenase and lactate dehydrogenase: Fact or misinterpretation? Proceedings of the National Academy of Sciences of the United States of America. 86: 6464-6468. PMID 2771937 |
0.155 |
|
| 1964 |
Shalitin Y, Bernhard SA. Neighboring group effects on ester hydrolysis. II. Neighboring carbonyl groups [6] Journal of the American Chemical Society. 86: 2292. |
0.152 |
|
| 1966 |
Bernhard SA, Lee BF, Tashjian ZH. On the interaction of the active side of alpha-chymotrypsin with chromophores: proflavin binding and enzyme conformation during catalysis. Journal of Molecular Biology. 18: 405-420. PMID 5966295 |
0.152 |
|
| 1987 |
Bernhard SA, Srivastava DK. Functional role of enzyme conformational changes in metabolism. Indian Journal of Biochemistry and Biophysics. 24: suppl 11-15. PMID 3329627 |
0.146 |
|
| 1978 |
Bernhard SA. Spectral intermediates in the activation of glyceraldehyde-3-PO(4)-dehydrogenase--catalyzed reactions. Biophysical Journal. 24: 49-53. PMID 213137 |
0.143 |
|
| 1987 |
Srivastava DK, Bernhard SA. Biophysical chemistry of metabolic reaction sequences in concentrated enzyme solution and in the cell. Annual Review of Biophysics and Biophysical Chemistry. 16: 175-204. PMID 3297086 |
0.141 |
|
| 1973 |
Seydoux F, Bernhard S, Pfenninger O, Payne M, Malhotra OP. Preparation and active-site specific properties of sturgeon muscle glyceraldehyde-3-phoshate dehydrogenase Biochemistry. 12: 4290-4300. PMID 4355559 DOI: 10.1021/bi00745a038 |
0.14 |
|
| 1971 |
Rossi GL, Bernhard SA. On the relationship between the conformation and the catalyzed reactivity of acyl-chymotrypsin Journal of Molecular Biology. 55: 215-230. PMID 5548605 DOI: 10.1016/0022-2836(71)90193-8 |
0.134 |
|
| 1985 |
Srivastava DK, Bernhard SA. Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Biochemistry. 24: 623-8. PMID 3158342 |
0.133 |
|
| 1970 |
Bernhard SA, Dunn MF, Luisi PL, Schack P. Mechanistic studies on equine liver alcohol dehydrogenase. I. The stoichiometry relationship of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient state Biochemistry. 9: 185-192. PMID 4312389 DOI: 10.1021/Bi00803A024 |
0.128 |
|
| 1978 |
Pattison S, Bernhard S. Functional consequences of ligand dependent conformational changes in trypsin solubilized and in membrane particle constrained acetylcholinesterase Proceedings of the National Academy of Sciences of the United States of America. 75: 3613-3617. PMID 278976 |
0.124 |
|
| 1956 |
BERNHARD SA. Ionization constants and heats of tris(hydroxymethyl)aminomethane and phosphate buffers. The Journal of Biological Chemistry. 218: 961-969. PMID 13295246 |
0.12 |
|
| 1979 |
Dunn MF, Bernhard SA, Anderson D, Copeland A, Morris RG, Roque JP. On site-site interactions in the liver alcohol dehydrogenase catalytic mechanism Biochemistry. 18: 2346-2354. PMID 221007 |
0.115 |
|
| 1964 |
Shalitin Y, Bernhard SA. Neighboring group effects on ester hydrolysis. I. Neighboring hydroxyl groups [5] Journal of the American Chemical Society. 86: 2291-2292. |
0.111 |
|
| 1971 |
MacQuarrie RA, Bernhard SA. Subunit conformation and catalytic function in rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase Journal of Molecular Biology. 55: 181-192. PMID 5102247 DOI: 10.1016/0022-2836(71)90190-2 |
0.108 |
|
| 1974 |
Seydoux F, Malhotra OP, Bernhard SA. Half-site reactivity. Crc Critical Reviews in Biochemistry. 2: 227-257. PMID 4366378 DOI: 10.3109/10409237409105448 |
0.106 |
|
| 1983 |
Bernhard SA. Nucleophilic displacement reactions at ester and thiolester bonds Annals of the New York Academy of Sciences. 28-40. PMID 6586102 |
0.102 |
|
| 1973 |
Bernhard SA, MacQuarrie RA. Half-site reactivity and the "induced-fit" hypothesis Journal of Molecular Biology. 74: 73-78. PMID 4731017 DOI: 10.1016/0022-2836(73)90356-2 |
0.101 |
|
| 1971 |
Bloch W, MacQuarrie RA, Bernhard SA. The nucleotide and acyl group content of native rabbit muscle glyceraldehyde 3-phosphate dehydrogenase. Journal of Biological Chemistry. 246: 780-790. PMID 5542690 |
0.1 |
|
| 1972 |
Bernhard SA, Lau S. Spectrophotometric and structural evidence as to the mechanism of portease catalysis at chemical bonding resolution. Cold Spring Harbor Symposia On Quantitative Biology. 36: 75-83. PMID 4508175 |
0.097 |
|
| 1955 |
BERNHARD SA. A new method for the determination of the amidase activity of trypsin: kinetics of the hydrolysis of benzoyl-L-arginineamide. The Biochemical Journal. 59: 506-9. PMID 14363128 |
0.096 |
|
| 1971 |
MacQuarrie RA, Bernhard SA. Mechanism of alkylation of rabbit muscle glyceraldehyde 3-phosphate dehydrogenase Biochemistry. 10: 2456-2466. PMID 4326767 |
0.091 |
|
| 1967 |
Charney E, Bernhard SA. Optical properties and the chemical nature of acyl-chymotrypsin linkages Journal of the American Chemical Society. 89: 2726-2733. PMID 6043802 |
0.089 |
|
| 1956 |
BERNHARD SA, GUTFREUND H. Ficincatalysed reactions: the affinity of ficin for some arginine derivatives. The Biochemical Journal. 63: 61-64. PMID 13315248 |
0.087 |
|
| 1965 |
Bernhard SA, Gutfreund H. The optical detection of transients in trypsin- and chymotrypsin-catalyzed reactions. Proceedings of the National Academy of Sciences of the United States of America. 53: 1238-1243. PMID 5217631 |
0.084 |
|
| 1966 |
Bernhard SA, Hershberger E, Keizer J. The influence of pH on the rate of hydrolysis of acylchymotrypsins Biochemistry. 5: 4120-4126. |
0.081 |
|
| 1974 |
Seydoux F, Bernhard S. On site heterogeneity in sturgeon muscle GPDH: a kinetic approach Biophysical Chemistry. 1: 161-174. PMID 4371889 DOI: 10.1016/0301-4622(74)80003-7 |
0.068 |
|
| 1972 |
McFarland JT, Bernhard SA. Catalytic steps during the single-turnover reduction of aldehydes by alcohol dehydrogenase Biochemistry. 11: 1486-1493. PMID 4336620 |
0.067 |
|
| 1950 |
Aston JG, Bernhard SA. Composition of the grignard reagent Nature. 165: 485. DOI: 10.1038/165485a0 |
0.065 |
|
| 1971 |
Rosenberry TL, Bernhard SA. Studies of catalysis by acetylcholinesterase. I. Fluorescent titration with a carbamoylating agent Biochemistry. 10: 4114-4120. PMID 5168614 |
0.05 |
|
| 1980 |
Inesi G, Kurzmack M, Nakamoto R, de Meis L, Bernhard SA. Uncoupling of calcium control and phosphohydrolase activity in sarcoplasmic reticulum vesicles. Journal of Biological Chemistry. 255: 6040-6043. PMID 6446552 |
0.041 |
|
| 1987 |
Bernhard SA, Srivastava DK. Functional consequences of the direct transfer of metabolites in muscle glycolysis. Biochemical Society Transactions. 15: 977-981. PMID 3691952 |
0.04 |
|
| 1955 |
Laidler KJ, Sturtevant JM, Laurence DJR, Gutfreund H, Neurath H, Lumry R, Rabin BR, Smith EL, Williams RJP, Robert L, Blum JJ, Bernhard SA, Bergmann F, Boyer PD, Davies DR, et al. General discussion Discussions of the Faraday Society. 20: 254-316. DOI: 10.1039/DF9552000254 |
0.013 |
|
| 1962 |
Bernhard SA, Duda WL. A Note on the Nature of RNA Codes [Letter to the Editor] Ibm Journal of Research and Development. 6: 365-367. DOI: 10.1147/rd.63.0365 |
0.01 |
|
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